DPH6_DANRE
ID DPH6_DANRE Reviewed; 255 AA.
AC A2RV01; Q5EAS1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Diphthine--ammonia ligase;
DE EC=6.3.1.14;
DE AltName: Full=ATP-binding domain-containing protein 4;
DE AltName: Full=Diphthamide synthase;
DE AltName: Full=Diphthamide synthetase;
DE AltName: Full=Protein DPH6 homolog;
GN Name=dph6; Synonyms=atpbd4; ORFNames=zgc:110758;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Amidase that catalyzes the last step of diphthamide
CC biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists
CC in the conversion of an L-histidine residue in the translation
CC elongation factor eEF-2 (EEF2) to diphthamide (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) =
CC AMP + diphosphate + diphthamide-[translation elongation factor 2] +
CC H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-
CC COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696,
CC ChEBI:CHEBI:456215; EC=6.3.1.14;
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2RV01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RV01-2; Sequence=VSP_024127;
CC -!- SIMILARITY: Belongs to the Diphthine--ammonia ligase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC090272; AAH90272.1; -; mRNA.
DR EMBL; BC133118; AAI33119.1; -; mRNA.
DR RefSeq; NP_001013308.2; NM_001013290.2. [A2RV01-1]
DR AlphaFoldDB; A2RV01; -.
DR SMR; A2RV01; -.
DR STRING; 7955.ENSDARP00000106089; -.
DR PaxDb; A2RV01; -.
DR PeptideAtlas; A2RV01; -.
DR Ensembl; ENSDART00000156774; ENSDARP00000129691; ENSDARG00000042839. [A2RV01-1]
DR GeneID; 503603; -.
DR KEGG; dre:503603; -.
DR CTD; 89978; -.
DR ZFIN; ZDB-GENE-050227-15; dph6.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR GeneTree; ENSGT00420000029820; -.
DR HOGENOM; CLU_010289_0_0_1; -.
DR InParanoid; A2RV01; -.
DR OMA; NYALYWA; -.
DR OrthoDB; 707303at2759; -.
DR PhylomeDB; A2RV01; -.
DR UniPathway; UPA00559; -.
DR PRO; PR:A2RV01; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000042839; Expressed in liver and 22 other tissues.
DR ExpressionAtlas; A2RV01; baseline.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IBA:GO_Central.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
DR CDD; cd01994; Alpha_ANH_like_IV; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR12196; PTHR12196; 1.
DR Pfam; PF01902; Diphthami_syn_2; 1.
DR PIRSF; PIRSF039123; Diphthamide_synthase; 1.
DR TIGRFAMs; TIGR00290; MJ0570_dom; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..255
FT /note="Diphthine--ammonia ligase"
FT /id="PRO_0000282400"
FT VAR_SEQ 39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024127"
FT CONFLICT 184
FT /note="L -> P (in Ref. 1; AAH90272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28401 MW; 131561D4D4D5196A CRC64;
MRVVGLISGG KDSCFNMLQC VSAGHSIVAL ANLRPADHAA SDELDSYMYQ TVGHQAVDLI
AEAMGLPLYR RTIEGSSVHI DREYSPTDGD EVEDLYQLLK HVKEEMHVDG VSVGAILSDY
QRVRVENVCA RLQLQPLAYL WRRDQAALLS EMISSGLHAI LIKVAAFGLH PDKHLGKSLA
EMELYLHELS EKYGVHICGE GGEYETFTLD CPLFKKKIII DATETVIHSD DAFAPVGFLR
FTKMHTEDKT EVRTL